Evidence map›Paper›PMID 21550976›Full record

ArticleThe Journal of biological chemistry2011

Functional and metabolic effects of adaptive glycerol kinase (GLPK) mutants in Escherichia coli.

M Kenyon Applebee, Andrew R Joyce, Tom M Conrad, Donald W Pettigrew, Bernhard Ø Palsson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 66 citations in OpenAlex.

  1. Aerobicity stimulon iniScience · 2026
    Article
  2. Review
  3. Enhanced nattokinase production byFrontiers in microbiology · 2025
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

M Kenyon ApplebeeDepartment of Chemistry & Biochemistry, University of California San Diego, La Jolla, California 92093, USA. mapplebe@ucsd.edu
Andrew R Joyce
Tom M Conrad
Donald W Pettigrew
Bernhard Ø Palsson
University of California, San Diego · USLa Jolla Bioengineering Institute · USTexas A&M University · US

Funding

Testable in silico Hypotheses for E.coli GrowthR01GM062791 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PALSSON, BERNHARD O · 2002 to 2009
$4.4M
NIGMS NIH HHS R01 GM062791NIGMS NIH HHS R01-GM062791-06
6 · The paper itself

Abstract

Herein we measure the effect of four adaptive non-synonymous mutations to the glycerol kinase (glpK) gene on catalytic function and regulation, to identify changes that correlate to increased fitness in glycerol media. The mutations significantly reduce affinity for the allosteric inhibitor fructose-1,6-bisphosphate (FBP) and formation of the tetramer, which are structurally related, in a manner that correlates inversely with imparted fitness during growth on glycerol, which strongly suggests that these enzymatic parameters drive growth improvement. Counterintuitively, the glpK mutations also increase glycerol-induced auto-catabolite repression that reduces glpK transcription in a manner that correlates to fitness. This suggests that increased specific GlpK activity is attenuated by negative feedback on glpK expression via catabolite repression, possibly to prevent methylglyoxal toxicity. We additionally report that glpK mutations were fixed in 47 of 50 independent glycerol-adapted lineages. By far the most frequently mutated locus (nucleotide 218) was mutated in 20 lineages, strongly suggesting this position has an elevated mutation rate. This study demonstrates that fitness correlations can be used to interrogate adaptive processes at the protein level and to identify the regulatory constraints underlying selection and improved growth.

Indexed as

Allosteric RegulationEscherichia coli K12Escherichia coli ProteinsFructosediphosphatesGlycerolGlycerol KinaseMutationEscherichia coli Proteinsfructose-1,6-diphosphateFructosediphosphatesGlycerolGlycerol Kinase

Identifiers

PMID21550976
PMCPMC3123082
OpenAlexW2047842052

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.